The CCP4 suite: programs for protein crystallography

Phaser crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Cancer-associated IDH1 mutations produce 2-hydroxyglutarate

Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154

Molecular basis of agonism and antagonism in the oestrogen receptor

Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206

Structural Basis of the Drug-binding Specificity of Human Serum Albumin

Ghuman, J., Zunszain, P. A., Petitpas, I., Bhattacharya, A. A., Otagiri, M., & Curry, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.075 · Cited by 1,941

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429

X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity

Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,446

Targeting tumor-associated macrophages with anti-CSF-1R antibody reveals a strategy for cancer therapy.

Ries, C. H., Cannarile, M. A., Hoves, S., Benz, J., Wartha, K., Runza, V., Rey-Giraud, F., Pradel, L. P., Feuerhake, F., Klaman, I., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.05.016 · Cited by 1,384

MR1 presents microbial vitamin B metabolites to MAIT cells

Kjer-Nielsen, L., Patel, O., Corbett, A. J., Le Nours, J., Meehan, B., Liu, L., Bhati, M., Chen, Z., Kostenko, L., Reantragoon, R., et al. (2012) · Nature · doi:10.1038/nature11605 · Cited by 1,351

Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247

Molecular Architecture of the Rotary Motor in ATP Synthase

Stock, D., Leslie, A. G. W., & Walker, J. E. (1999) · Science · doi:10.1126/science.286.5445.1700 · Cited by 1,271

Structure of TPR Domain–Peptide Complexes

Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188

Helical Assembly in the MyD88-IRAK4-IRAK2 Complex in TLR/IL-1R Signalling

Lin, S.-C., Lo, Y.-C., & Wu, H. (2010) · Nature · doi:10.1038/nature09121 · Cited by 1,111

mTOR kinase structure, mechanism and regulation

Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., & Pavletich, N. P. (2013) · Nature · doi:10.1038/nature12122 · Cited by 1,075

Crystal structure of opsin in its G-protein-interacting conformation

Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059

Latent TGF-β structure and activation

Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013

Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979

The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit

Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951

Structure of mammalian AMPK and its regulation by ADP

Xiao, B., Sanders, M. J., Underwood, E., Heath, R., Mayer, F. V., Carmena, D., Jing, C., Walker, P. A., Eccleston, J. F., Haire, L. F., et al. (2011) · Nature · doi:10.1038/nature09932 · Cited by 926

Crystal Structure of a Laccase from the FungusTrametes versicolor at 1.90-Å Resolution Containing a Full Complement of Coppers

Piontek, K., Antorini, M., & Choinowski, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204571200 · Cited by 909

Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker

Solca, F., Dahl, G., Zoephel, A., Bader, G., Sanderson, M., Klein, C., Kraemer, O., Himmelsbach, F., Haaksma, E., & Adolf, G. R. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.197756 · Cited by 865

Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864

Structure of a c-Cbl–UbcH7 Complex

Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839

The physiological structure of human C-reactive protein and its complex with phosphocholine

Thompson, D., Pepys, M. B., & Wood, S. P. (1999) · Structure · doi:10.1016/s0969-2126(99)80023-9 · Cited by 818

The structural basis of the activation of Ras by Sos

Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., & Kuriyan, J. (1998) · Nature · doi:10.1038/28548 · Cited by 799

Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA

Chandra, V., Huang, P., Hamuro, Y., Raghuram, S., Wang, Y., Burris, T. P., & Rastinejad, F. (2008) · Nature · doi:10.1038/nature07413 · Cited by 808

Crystal structure of the entire respiratory complex I

Baradaran, R., Berrisford, J. M., Minhas, G. S., & Sazanov, L. A. (2013) · Nature · doi:10.1038/nature11871 · Cited by 797

Crystal structure of the human glucose transporter GLUT1

Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., & Yan, N. (2014) · Nature · doi:10.1038/nature13306 · Cited by 777

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Zhou, T., Xu, L., Dey, B., Hessell, A. J., Van Ryk, D., Xiang, S.-H., Yang, X., Zhang, M.-Y., Zwick, M. B., Arthos, J., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770

Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose

Ferrara, C., Grau, S., Jäger, C., Sondermann, P., Brünker, P., Waldhauer, I., Hennig, M., Ruf, A., Rufer, A. C., Stihle, M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108455108 · Cited by 770

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751

Energetic optimization of ion conduction rate by the K+ selectivity filter

Morais-Cabral, J. H., Zhou, Y., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102000 · Cited by 761

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697

Mammalian Microsomal Cytochrome P450 Monooxygenase

Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

Pejchal, R., Doores, K. J., Walker, L. M., Khayat, R., Huang, P.-S., Wang, S.-K., Stanfield, R. L., Julien, J.-P., Ramos, A., Crispin, M., et al. (2011) · Science · doi:10.1126/science.1213256 · Cited by 694

Retroviral intasome assembly and inhibition of DNA strand transfer

Hare, S., Gupta, S. S., Valkov, E., Engelman, A., & Cherepanov, P. (2010) · Nature · doi:10.1038/nature08784 · Cited by 678

Targeting C-reactive protein for the treatment of cardiovascular disease.

Pepys, M. B., Hirschfield, G. M., Tennent, G. A., Ruth Gallimore, J., Kahan, M. C., Bellotti, V., Hawkins, P. N., Myers, R. M., Smith, M. D., Polara, A., et al. (2006) · Nature · doi:10.1038/nature04672 · Cited by 672

Crystal structure of metarhodopsin II

Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663

Serine is a natural ligand and allosteric activator of pyruvate kinase M2

Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661

Simultaneous Binding of PtdIns(4,5)P 2 and Clathrin by AP180 in the Nucleation of Clathrin Lattices on Membranes

Ford, M. G. J., Pearse, B. M. F., Higgins, M. K., Vallis, Y., Owen, D. J., Gibson, A., Hopkins, C. R., Evans, P. R., & McMahon, H. T. (2001) · Science · doi:10.1126/science.291.5506.1051 · Cited by 659

High-affinity binders selected from designed ankyrin repeat protein libraries

Binz, H. K., Amstutz, P., Kohl, A., Stumpp, M. T., Briand, C., Forrer, P., Grütter, M. G., & Plückthun, A. (2004) · Nature Biotechnology · doi:10.1038/nbt962 · Cited by 656

Structural basis for androgen specificity and oestrogen synthesis in human aromatase

Ghosh, D., Griswold, J., Erman, M., & Pangborn, W. (2009) · Nature · doi:10.1038/nature07614 · Cited by 618

Structural Evidence for Ligand Specificity in the Binding Domain of the Human Androgen Receptor

Matias, P. M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Macedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004571200 · Cited by 608

Crystal structure of the outer membrane active transporter FepA from Escherichia coli.

Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591

Structural basis for AMP binding to mammalian AMP-activated protein kinase

Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., Walker, P. A., Haire, L., Eccleston, J. F., Davis, C. T., et al. (2007) · Nature · doi:10.1038/nature06161 · Cited by 591

Redesigning an FKBP–ligand interface to generate chemical dimerizers with novel specificity

Clackson, T., Yang, W., Rozamus, L. W., Hatada, M., Amara, J. F., Rollins, C. T., Stevenson, L. F., Magari, S. R., Wood, S. A., Courage, N. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10437 · Cited by 558

IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding

Hymowitz, S. G., Filvaroff, E. H., Yin, J., Lee, J., Cai, L., Risser, P., Maruoka, M., Mao, W., Foster, J., Kelley, R. F., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.19.5332 · Cited by 548

Molecular model for a complete clathrin lattice from electron cryomicroscopy

Fotin, A., Cheng, Y., Sliz, P., Grigorieff, N., Harrison, S. C., Kirchhausen, T., & Walz, T. (2004) · Nature · doi:10.1038/nature03079 · Cited by 541

BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design

Farnaby, W., Koegl, M., Roy, M. J., Whitworth, C., Diers, E., Trainor, N., Zollman, D., Steurer, S., Karolyi-Oezguer, J., Riedmueller, C., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0294-6 · Cited by 562

Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a

Russo, A. A., Tong, L., Lee, J.-O., Jeffrey, P. D., & Pavletich, N. P. (1998) · Nature · doi:10.1038/26155 · Cited by 524

Pan-KRAS Inhibitor Disables Oncogenic Signalling and Tumour Growth

Kim, D., Herdeis, L., Rudolph, D., Zhao, Y., Böttcher, J., Vides, A., Ayala-Santos, C. I., Pourfarjam, Y., Cuevas-Navarro, A., Xue, J. Y., et al. (2023) · Nature · doi:10.1038/s41586-023-06123-3 · Cited by 534

Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

Chen, L., Glover, J. N. M., Hogan, P. G., Rao, A., & Harrison, S. C. (1998) · Nature · doi:10.1038/32100 · Cited by 521

Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate

Watson, P. J., Fairall, L., Santos, G. M., & Schwabe, J. W. R. (2012) · Nature · doi:10.1038/nature10728 · Cited by 505

cGAS senses long and HMGB/TFAM-bound U-turn DNA by forming protein-DNA ladders

Andreeva, L., Hiller, B., Kostrewa, D., Lässig, C., de Oliveira Mann, C. C., Jan Drexler, D., Maiser, A., Gaidt, M., Leonhardt, H., Hornung, V., et al. (2017) · Nature · doi:10.1038/nature23890 · Cited by 511

Structure of a cytochrome P450-redox partner electron-transfer complex

Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501

Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491

Cooperative binding of two acetylation marks on a histone tail by a single bromodomain

Morinière, J., Rousseaux, S., Steuerwald, U., Soler-López, M., Curtet, S., Vitte, A.-L., Govin, J., Gaucher, J., Sadoul, K., Hart, D. J., et al. (2009) · Nature · doi:10.1038/nature08397 · Cited by 469

Structure of the LDL Receptor Extracellular Domain at Endosomal pH

Rudenko, G., Henry, L., Henderson, K., Ichtchenko, K., Brown, M. S., Goldstein, J. L., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1078124 · Cited by 482

Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication

Christ, F., Voet, A., Marchand, A., Nicolet, S., Desimmie, B. A., Marchand, D., Bardiot, D., Van der Veken, N. J., Van Remoortel, B., Strelkov, S. V., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.370 · Cited by 479

Structural insight into filament formation by mammalian septins

Sirajuddin, M., Farkasovsky, M., Hauer, F., Kühlmann, D., Macara, I. G., Weyand, M., Stark, H., & Wittinghofer, A. (2007) · Nature · doi:10.1038/nature06052 · Cited by 481

Site-directed ligand discovery

Erlanson, D. A., Braisted, A. C., Raphael, D. R., Randal, M., Stroud, R. M., Gordon, E. M., & Wells, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9367 · Cited by 466

The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation

Fischer, E. S., Scrima, A., Böhm, K., Matsumoto, S., Lingaraju, G. M., Faty, M., Yasuda, T., Cavadini, S., Wakasugi, M., Hanaoka, F., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.035 · Cited by 460

Structure of a complex of the ATPase SecA and the protein-translocation channel.

Zimmer, J., Nam, Y., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07335 · Cited by 459

Gantenerumab: A Novel Human Anti-Aβ Antibody Demonstrates Sustained Cerebral Amyloid-β Binding and Elicits Cell-Mediated Removal of Human Amyloid-β

Bohrmann, B., Baumann, K., Benz, J., Gerber, F., Huber, W., Knoflach, F., Messer, J., Oroszlan, K., Rauchenberger, R., Richter, W. F., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110977 · Cited by 448

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.

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Crystal structure of a photoactivated deprotonated intermediate of rhodopsin

Salom, D., Lodowski, D. T., Stenkamp, R. E., Trong, I. L., Golczak, M., Jastrzebska, B., Harris, T., Ballesteros, J. A., & Palczewski, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608022103 · Cited by 442

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Groves, M. R., Hanlon, N., Turowski, P., Hemmings, B. A., & Barford, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80963-0 · Cited by 442

Structure of a unique binuclear manganese cluster in arginase

Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996) · Nature · doi:10.1038/383554a0 · Cited by 441

Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex

Scrima, A., Koníčková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., & Thomä, N. H. (2008) · Cell · doi:10.1016/j.cell.2008.10.045 · Cited by 441

Chloride sensing by WNK1 involves inhibition of autophosphorylation

Piala, A. T., Moon, T. M., Akella, R., He, H., Cobb, M. H., & Goldsmith, E. J. (2014) · Science Signaling · doi:10.1126/scisignal.2005050 · Cited by 418

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J. M., Delarue, M., & Corringer, P.-J. (2011) · Nature · doi:10.1038/nature09647 · Cited by 412

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75

Cherepanov, P., Ambrosio, A. L. B., Rahman, S., Ellenberger, T., & Engelman, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506924102 · Cited by 408

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

Cunningham, D., Danley, D. E., Geoghegan, K. F., Griffor, M. C., Hawkins, J. L., Subashi, T. A., Varghese, A. H., Ammirati, M. J., Culp, J. S., Hoth, L. R., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1235 · Cited by 409

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding

Chen, J. C.-H., Krucinski, J., Miercke, L. J. W., Finer-Moore, J. S., Tang, A. H., Leavitt, A. D., & Stroud, R. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150220297 · Cited by 404

Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α11Edited by K. Nagai

Fontes, M. R. M., Teh, T., & Kobe, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3642 · Cited by 398

Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α

Elkins, J. M., Hewitson, K. S., McNeill, L. A., Seibel, J. F., Schlemminger, I., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200644200 · Cited by 391

Molecular basis for LDL receptor recognition by PCSK9

Kwon, H. J., Lagace, T. A., McNutt, M. C., Horton, J. D., & Deisenhofer, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712064105 · Cited by 389

Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function

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Crystal Structure of the CSL-Notch-Mastermind Ternary Complex Bound to DNA

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